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Literature summary extracted from
- Investigation of interaction between enolase and phosphoglycerate mutase using molecular dynamics simulation (2006), J. Biomol. Struct. Dyn., 23, 625-633.
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | Saccharomyces cerevisiae | - |
phosphoenolpyruvate + H2O | - |
r |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.11 | Saccharomyces cerevisiae | P00924 | - |
- |
| 5.4.2.11 | Saccharomyces cerevisiae | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.11 | additional information | - |
binding affinity between enolase and phosphoglycerate mutase confirmed by interaction energies and conformation changes, 10 A resolution and three orientations positioning enolase towards to phosphoglycerate mutase tested in presence of 150 mM NaCl | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.11 | 2-phospho-D-glycerate | - |
Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r | |
| 4.2.1.11 | 2-phospho-D-glycerate | direct transfer mechanisms of substrates between enolase and phosphoglycerate mutase predicted by molecular dynamics simulation | Saccharomyces cerevisiae | phosphoenolpyruvate + H2O | - |
r | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.2.11 | More | molecular dynamics simulation reveals that the enzyme interacts with its C-terminal domain with enolase, suggesting a direct transfer mechanism of substrate | Saccharomyces cerevisiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.1.11 | enolase | - |
Saccharomyces cerevisiae |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.2.1.11 | additional information | complex formation between active centers of enolase and phosphoglycerate mutase determined, interaction of enolase with C-terminal tail of phosphoglycerate mutase confirmed | Saccharomyces cerevisiae |
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